ID   ETKMT_RAT               Reviewed;         255 AA.
AC   Q6P7Q0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q80ZM3, ECO:0000250|UniProtKB:Q8IXQ9};
DE   AltName: Full=ETFB lysine methyltransferase;
DE            Short=ETFB-KMT;
DE   AltName: Full=Protein N-lysine methyltransferase METTL20;
DE   Flags: Precursor;
GN   Name=Etfbkmt {ECO:0000312|RGD:735147}; Synonyms=Mettl20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC       trimethylates the flavoprotein ETFB in mitochondria. Thereby, may
CC       negatively regulate the function of ETFB in electron transfer from
CC       Acyl-CoA dehydrogenases to the main respiratory chain.
CC       {ECO:0000250|UniProtKB:Q8IXQ9}.
CC   -!- SUBUNIT: Interacts with HSPD1; this protein may possibly be a
CC       methylation substrate. {ECO:0000250|UniProtKB:Q8IXQ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ9}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IXQ9}. Note=Concentrated
CC       in cytoplasmic granular foci. {ECO:0000250|UniProtKB:Q8IXQ9}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. ETFBKMT
CC       family. {ECO:0000305}.
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DR   EMBL; BC061574; AAH61574.1; -; mRNA.
DR   RefSeq; NP_942067.1; NM_198772.1.
DR   RefSeq; XP_006237763.1; XM_006237701.3.
DR   AlphaFoldDB; Q6P7Q0; -.
DR   SMR; Q6P7Q0; -.
DR   STRING; 10116.ENSRNOP00000052309; -.
DR   PaxDb; Q6P7Q0; -.
DR   Ensembl; ENSRNOT00000055442; ENSRNOP00000052309; ENSRNOG00000036918.
DR   GeneID; 316976; -.
DR   KEGG; rno:316976; -.
DR   UCSC; RGD:735147; rat.
DR   CTD; 254013; -.
DR   RGD; 735147; Etfbkmt.
DR   eggNOG; ENOG502QUSY; Eukaryota.
DR   GeneTree; ENSGT00940000162982; -.
DR   HOGENOM; CLU_074455_2_1_1; -.
DR   InParanoid; Q6P7Q0; -.
DR   OMA; ILNCELN; -.
DR   OrthoDB; 1585716at2759; -.
DR   PhylomeDB; Q6P7Q0; -.
DR   TreeFam; TF314934; -.
DR   Reactome; R-RNO-8876725; Protein methylation.
DR   PRO; PR:Q6P7Q0; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000036918; Expressed in heart and 19 other tissues.
DR   Genevisible; Q6P7Q0; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR   GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:1904733; P:negative regulation of electron transfer activity; ISS:UniProtKB.
DR   GO; GO:1904736; P:negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; ISO:RGD.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXQ9"
FT   CHAIN           33..255
FT                   /note="Electron transfer flavoprotein beta subunit lysine
FT                   methyltransferase"
FT                   /id="PRO_0000318711"
SQ   SEQUENCE   255 AA;  28641 MW;  4674023BDA536729 CRC64;
     MAFSLCWKAP RSQWSFLQAL NSGFPLFPWR TVGSCLDLKM KAYLEENTEV TSSGSLTPEI
     QLRLLTPRCK FWWERADLWP YSDPYWAIYW PGGQALSRYL LDNPDVVRGK SVLDLGSGCG
     ATAIAAKMSG ASNILANDVD PIAGMAITLN CKLNGLNPFP ILTKNILNTR QGKFDLIVLG
     DMFYDEDLAD SLHLWLQNCF WAYGTRVLIG DPGRPQFSGH SIQHQLYQLA EYTLPEPTQQ
     DNNGLTTSAV WDFHP